Heme-carbonyl
complexes are widely exploited for the insight they
provide into the structural basis of function in heme-based proteins,
by revealing the nature of their bonded and nonbonded interactions
with the protein. This report presents two novel results which clearly
establish a FeCO vibrational signature for crystallographically verified
pentacoordination. First, anisotropy in the NRVS density of states
for νFe–C and δFeCO in oriented
single crystals of [Fe(OEP)(CO)] clearly reveals that the Fe–C
stretch occurs at higher frequency than the FeCO bend and considerably
higher than any previously reported heme carbonyl. Second, DFT calculations
on a series of heme carbonyls reveal that the frequency crossover
occurs near the weak trans O atom donor, furan. As
νFe–C occurs at lower frequencies than δFeCO in all heme protein carbonyls reported to date, the results
reported herein suggest that they are all hexacoordinate.